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Biochem Biophys Res Commun. 1997 Nov 17;240(2):335-40.

Cloning and characterization of a putative human RNA helicase gene of the DEAH-box protein family.

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AGENE Research Institute, Kamakura, Japan.


A human RNA helicase gene, DBP1, was cloned by PCR methodsusing degenerate oligonucleotide primers corresponding to highly conserved motifs among known members of the DEAH-box protein family. The full-length DBP1 contains 3028 nucleotides and codes for a protein of 813 amino acids with a calculated mol. wt. of 92723 daltons. The predicted amino acid sequence shares extensive homology with Prp2, Prp16, and Prp22 proteins, which are required to splice mRNA precursors in budding yeast. The protein encoded by DBP1 has RGD, RD, and HS(A/T) repeat motifs close to the N-terminus. Southern blot analysis suggested the presence of a homologue of the DBP1 genes in other species, and Northern blot analysis showed that DBP1 is expressed ubiquitously in various human organs investigated. The DBP1 gene was found to be on chromosome 4p15.3 and encodes a putative nuclear ATP-dependent RNA helicase.

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